Reviewed, UniProtKB/Swiss-Prot P09110 (THIK_HUMAN)

Names and origin

Protein names

Recommended name:
    3-ketoacyl-CoA thiolase, peroxisomal
    EC=2.3.1.16
Alternative name(s):
    Beta-ketothiolase
    Acetyl-CoA acyltransferase
    Peroxisomal 3-oxoacyl-CoA thiolase

Gene names

Name:	ACAA1
Synonyms:	ACAA, PTHIO

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	424 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.
Pathway	Lipid metabolism; fatty acid metabolism.
Subunit structure	Homodimer. Ref.7
Subcellular location	Peroxisome.
Induction	Peroxisomal thiolase is markedly induced (at the level of transcription) by various hypolipidemic compounds in parallel with the other two enzymes of the peroxisomal beta-oxidation system.
Sequence similarities	Belongs to the thiolase family.

Ontologies

Keywords
Biological process	Fatty acid metabolism Lipid metabolism
Cellular component	Peroxisome
Coding sequence diversity	Polymorphism
Domain	Transit peptide
Molecular function	Acyltransferase Transferase
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	fatty acid metabolic process Inferred from electronic annotation. Source: UniProtKB-KW generation of precursor metabolites and energy Ref.4 Traceable author statement. Source: ProtInc
Cellular component	peroxisome Ref.4 Non-traceable author statement. Source: ProtInc
Molecular function	acetyl-CoA C-acyltransferase activity Inferred from electronic annotation. Source: EC protein binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 26

26

Peroxisome

Chain

27 – 424

398

3-ketoacyl-CoA thiolase, peroxisomal

PRO_0000034067

Sites

Active site

123

1

Acyl-thioester intermediate By similarity

Active site

377

1

Proton acceptor By similarity

Active site

408

1

Proton acceptor By similarity

Natural variations

Natural variant

172

1

E → D: dbSNP rs156265.

VAR_011904

Secondary structure

1

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424

Helix Strand Turn

Details...

Beta strand

38 – 45

8

Turn

51 – 53

3

Turn

55 – 58

4

Helix

61 – 76

16

Helix

80 – 82

3

Beta strand

86 – 89

4

Beta strand

91 – 94

4

Helix

95 – 97

3

Helix

98 – 107

10

Beta strand

116 – 120

5

Helix

122 – 124

3

Helix

125 – 138

14

Beta strand

143 – 152

10

Turn

153 – 155

3

Helix

168 – 170

3

Helix

172 – 175

4

Helix

176 – 178

3

Helix

181 – 191

11

Helix

196 – 216

21

Turn

217 – 222

6

Beta strand

226 – 231

6

Beta strand

237 – 242

6

Helix

254 – 259

6

Beta strand

263 – 265

3

Beta strand

279 – 289

11

Helix

290 – 296

7

Beta strand

302 – 311

10

Helix

314 – 319

6

Helix

320 – 332

13

Helix

336 – 338

3

Beta strand

339 – 344

6

Helix

349 – 359

11

Helix

363 – 365

3

Helix

372 – 375

4

Turn

379 – 381

3

Helix

382 – 397

16

Beta strand

401 – 409

9

Turn

410 – 412

3

Beta strand

413 – 421

9

Sequences

	Sequence		Length	Mass (Da)
	P09110-1 [UniParc]. Last modified October 1, 1989. Version 2. Checksum: 71B2BBAFA06AE412	FASTA	424	44,292
	10 20 30 40 50 60 MQRLQVVLGH LRGPADSGWM PQAAPCLSGA PQASAADVVV VHGRRTAICR AGRGGFKDTT 70 80 90 100 110 120 PDELLSAVMT AVLKDVNLRP EQLGDICVGN VLQPGAGAIM ARIAQFLSDI PETVPLSTVN 130 140 150 160 170 180 RQCSSGLQAV ASIAGGIRNG SYDIGMACGV ESMSLADRGN PGNITSRLME KEKARDCLIP 190 200 210 220 230 240 MGITSENVAE RFGISREKQD TFALASQQKA ARAQSKGCFQ AEIVPVTTTV HDDKGTKRSI 250 260 270 280 290 300 TVTQDEGIRP STTMEGLAKL KPAFKKDGST TAGNSSQVSD GAAAILLARR SKAEELGLPI 310 320 330 340 350 360 LGVLRSYAVV GVPPDIMGIG PAYAIPVALQ KAGLTVSDVD IFEINEAFAS QAAYCVEKLR 370 380 390 400 410 420 LPPEKVNPLG GAVALGHPLG CTGARQVITL LNELKRRGKR AYGVVSMCIG TGMGAAAVFE YPGN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of human peroxisomal 3-oxoacyl-CoA thiolase." Bout A., Teunissen Y., Hashimoto T., Benne R., Tager J.M. Nucleic Acids Res. 16:10369-10369(1988) [PubMed: 3194209] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[2]	Bout A. Submitted (AUG-1989) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 285-287.
[3]	"Complete cDNA sequence of human foetal liver peroxisomal 3-oxoacyl-CoA thiolase." Fairbairn L.J., Tanner M.J.A. Nucleic Acids Res. 17:3588-3588(1989) [PubMed: 2726492] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Liver.
[4]	"Characterization of the gene encoding human peroxisomal 3-oxoacyl-CoA thiolase (ACAA). No large DNA rearrangement in a thiolase-deficient patient." Bout A., Franse M.M., Collins J., Blonden L., Tager J.M., Benne R. Biochim. Biophys. Acta 1090:43-51(1991) [PubMed: 1679347] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lymph and Ovary.
[6]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[7]	"Crystal structure of human peroxisomal acetyl-COA acyl transferase 1 (ACAA1)." Structural genomics consortium (SGC) Submitted (OCT-2006) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 28-424, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X12966 mRNA. Translation: CAA31412.1.
X14813 mRNA. Translation: CAA32918.1.
X65140 Genomic DNA. Translation: CAA46270.1.
X65148 Genomic DNA. Translation: CAA46271.1.
BC000635 mRNA. Translation: AAH00635.1.
BC011977 mRNA. Translation: AAH11977.1.

IPI

IPI00012828.

PIR

XUHUAB. S17515.

RefSeq

NP_001598.1.

UniGene

Hs.643487

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2IIK	X-ray	2.55	A/B	30-423	[»]

ModBase

Search...

2-D gel databases

REPRODUCTION-2DPAGE

IPI00012828.

Proteomic databases

PeptideAtlas

P09110.

PRIDE

P09110.

Genome annotation databases

Ensembl

ENSG00000060971. Homo sapiens. [Contig view]

GeneID

30.

NMPDR

fig|9606.3.peg.22303.

UCSC

uc003cht.1. human.

Organism-specific databases

GeneCards

GC03M038139.

HGNC

HGNC:82. ACAA1.

HPA

HPA006764.
HPA007244.

MIM

604054. gene.

Orphanet

2981. Pseudo-Zellweger syndrome.

PharmGKB

PA24419.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P09110.

HOVERGEN

P09110.

OMA

P09110. PNTTMEG.

Enzyme and pathway databases

BRENDA

2.3.1.16. 247.

Reactome

REACT_602. Metabolism of lipids and lipoproteins.

Gene expression databases

ArrayExpress

P09110.

Bgee

P09110.

CleanEx

HS_ACAA1.

GermOnline

ENSG00000060971. Homo sapiens.

Family and domain databases

InterPro

IPR002155. Thiolase.
IPR016038. Thiolase-like_subgr.
[Graphical view]

Gene3D

G3DSA:3.40.47.10. Thiolase-like_subgr. 1 hit.

PANTHER

PTHR18919. Thiolase. 1 hit.

Pfam

PF02803. Thiolase_C. 1 hit.
PF00108. Thiolase_N. 1 hit.
[Graphical view]

PIRSF

PIRSF000429. Ac-CoA_Ac_transf. 1 hit.

TIGRFAMs

TIGR01930. AcCoA-C-Actrans. 1 hit.

PROSITE

PS00098. THIOLASE_1. 1 hit.
PS00737. THIOLASE_2. 1 hit.
PS00099. THIOLASE_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

107.

SOURCE

Search...

Entry information

Entry name

THIK_HUMAN

Accession

Primary (citable) accession number: P09110

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	October 1, 1989
Last modified:	July 7, 2009
This is version 113 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)